Globular-shaped variable lymphocyte receptors B antibody multimerized by a hydrophobic clustering in hagfish

Scientific Reports
Jaesung KimTae Sung Jung

Abstract

In hagfish and lampreys, two representative jawless vertebrates, the humoral immunity is directly mediated by variable lymphocyte receptors B (VLRBs). Both monomeric VLRBs are structurally and functionally similar, but their C-terminal tails differ: lamprey VLRB has a Cys-rich tail that forms disulfide-linked pentamers of dimers, contributing to its multivalency, whereas hagfish VLRB has a superhydrophobic tail of unknown structure. Here, we reveal that VLRBs obtained from hagfish plasma have a globular-shaped multimerized form (approximately 0.6 to 1.7 MDa) that is generated by hydrophobic clustering instead of covalent linkage. Electron microscopy (EM) and single-particle analysis showed that the multimerized VLRBs form globular-shaped clusters with an average diameter of 28.7 ± 2.2 nm. The presence of VLRBs in the complex was confirmed by immune-EM analysis using an anti-VLRB antibody. Furthermore, the hydrophobic hagfish C-terminus (HC) was capable of triggering multimerization and directing the cellular surface localization via a glycophosphatidylinositol linkage. Our results strongly suggest that the hagfish VLRB forms a previously unknown globular-shaped antibody. This novel identification of a structurally unusual VLRB ...Continue Reading

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Citations

Dec 15, 2019·The Journal of Immunology : Official Journal of the American Association of Immunologists·Jae Wook JungTae Sung Jung
Apr 23, 2020·International Journal of Molecular Sciences·Si Won KimTae Sung Jung

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Methods Mentioned

BETA
size-exclusion chromatography
dot blotting
gel filtration
transmission electron microscopy
size-exclusion
flow cytometry
FACS
ELISA
Protein Assay
electrophoresis

Software Mentioned

SPIDER

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